Showing papers on "Heat shock protein published in 1978"
TL;DR: Several laboratories have reported synthesis of proteins with similar molecular weights in cells subjected to conditions that alter glucose metabolism, and it is speculated that these proteins may be associated with a hexose transport system.
499 citations
TL;DR: The heat shock loci of Drosophila melanogaster chromosome subdivisions 87A and 87C have been studied by using cloned DNA and in situ hybridization to chromosomal RNA shows that transcripts of this sequence accumulate at both sites after temperature elevation.
Abstract: The heat shock loci of Drosophila melanogaster chromosome subdivisions 87A and 87C have been studied by using cloned DNA. Both sites contain a number of copies of a 2,4-kilobase (kb) region homologous to mRNA for the 70,000-dalton heat shock protein. In situ hybridization to chromosomal RNA shows that transcripts of this sequence accumulate at both sites after temperature elevation. At 87C there is a 1.5-kb repeated sequence homologous to another heat shock RNA. One cloned segment includes two to three tandem copies of this sequence located 0.8 kb from the beginning of a 2.4-kb message region. RNA complementary to the 1.5-kb repeat acccumulates at 87C after temperature elevation, but does not code for any known heat shock protein. In the sibling species D. simulans, there are sequences located and transcribed at 87A and 87C that are homologous to the melanogaster 2.4-kb message sequence. The 1.5-kb repeat, however, is absent from 87C in simulans and no heat shock RNA homologous to it can be detected.
147 citations
TL;DR: Two cloned segments of Drosophila melanogaster DNA containing "heat shock" gene sequences hybridize in situ to the heat-induced puff sites located at 87A and 87C of the salivary gland polytene chromosomes.
119 citations
TL;DR: Differentiation of the single cells that yield bristles and hairs in Drosophila has been examined by studies of phenocopies induced by heat shock and may be related to heat shock effects on RNA synthesis through a feedback inhibition of transcription by heatshock proteins.
102 citations
TL;DR: The heat shock proteins, labelled in vivo with [35S]methionine, were separated by sodium dodecylsulphate-polyacrylamide gel electrophoresis and fingerprinted after tryptic digestion to characterize eight distinct heat shock polypeptides.
Abstract: The heat shock proteins, labelled in vivo with [35S]methionine, were separated by sodium dodecylsulphate-polyacrylamide gel electrophoresis and fingerprinted after tryptic digestion. Eight distinct heat shock polypeptides are characterized in this way. Heat shock messenger RNAs were isolated and partially purified. Assayed in vitro for protein synthesis, they were found to code for heat shock polypeptides. Some parameters of the kinetics of in vivo synthesis of the heat shock proteins are presented.
63 citations
TL;DR: SDS-polyacrylamide gel electrophoresis revealed similar distributions of heat shock proteins in the two species studied, and concluded that region 29C of D. virilis contains DNA sequences retaining molecular homology with those at subdivisions 87A and 87Cl ofD.
Abstract: Polytene chromosomes of D. melanogaster and D. virilis were hybridized in situ with 125I labeled mRNA isolated from polysomes of D. melanogaster tissue culture cells incubated at 37° C. 125I mRNA hybridized preferentially with subdivisions 87A and 87Cl of the D. melanogaster 3R chromosome; grains were also observed at regions 93D, 95D and over the chromocenter. A considerable cross hybridization of this mRNA with D. virilis polytene chromosomes was observed. The 29C region of the D. virilis second chromosome was the main site of hybridization. Significant grain numbers also appeared in region 20F of the same chromosome. The two regions mentioned belong to heat shock loci in the latter species. Based on label intensity we conclude that region 29C of D. virilis contains DNA sequences retaining molecular homology with those at subdivisions 87A and 87Cl of D. melanogaster. SDS-polyacrylamide gel electrophoresis revealed similar distributions of heat shock proteins in the two species studied.
25 citations
01 Jan 1978
13 citations